Wide Diversity and Complex Evolution of M42 Aminopeptidases With Contrasted Functional Properties in Archaea.

ABSTRACT: M42 peptidases (TET) are ubiquitous, giant self-compartmentalized aminopeptidases forming unique tetrahedral structures. TETs may participate in protein homeostasis and amino acid recycling by processing peptides downstream of the proteasome and other related proteolytic complexes. Currently, only five TETs have been extensively studied in Archaea from the Thermococcales order, with a predominant focus on structural characterization. Therefore, a clear view of the diversity and biological activities of this large enzymatic family is lacking. In this study, we establish robust criteria for high-throughput identification of TET peptidases from sequence data and reveal their wide taxonomic distribution in Archaea. We functionally characterize six additional TETs, including four from Asgardarc

SUBMITTER: Chagny E 

PROVIDER: S-EPMC12516491 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature